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Q9UBU9 (NXF1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 159. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Nuclear RNA export factor 1
Alternative name(s):
Tip-associated protein
Tip-associating protein
mRNA export factor TAP
Gene names
Name:NXF1
Synonyms:TAP
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length619 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in the nuclear export of mRNA species bearing retroviral constitutive transport elements (CTE) and in the export of mRNA from the nucleus to the cytoplasm (TAP/NFX1 pathway). The NXF1-NXT1 heterodimer is involved in the export of HSP70 mRNA in conjunction with ALYREF/THOC4 and THOC5 components of the TREX complex. ALYREF/THOC4-bound mRNA is thought to be transferred to the NXF1-NXT1 heterodimer for export. Ref.9 Ref.18 Ref.21

Subunit structure

Heterodimer with NXT1. Interacts (via NTF2 domain) with NXT1. The formation of NXF1-NXT1 heterodimers is required for the NXF1-mediated nuclear mRNA export. Interacts with NXT2, E1B-AP5, RAE1, ALYREF/THOC4, DDX39B, FYTTD1/UIF, EIF4A3, NUPL2 and with several nucleoporins. Interacts with THOC5 and CHTOP; in a mutually exclusive manner. Associates with the exon junction complex (EJC) and with the transcription/export (TREX) complex. Found in a mRNA complex with RENT3A and RENT3B. Interacts with Saimiriine herpesvirus 2 TIP protein. Interacts with human herpes virus 1 (HHV-1) ICP27 protein; this interaction allows efficient export of HHV-1 early and late transcripts. Ref.8 Ref.10 Ref.14 Ref.15 Ref.16 Ref.17 Ref.20 Ref.21 Ref.23 Ref.26 Ref.27 Ref.29

Subcellular location

Nucleusnucleoplasm. Nucleus speckle. Cytoplasm. Note: Localized predominantly in the nucleoplasm and at both the nucleoplasmic and cytoplasmic faces of the nuclear pore complex. Shuttles between the nucleus and the cytoplasm. Travels to the cytoplasm as part of the exon junction complex (EJC) bound to mRNA. The association with the TREX complex seems to occur in regions surrounding nuclear speckles known as perispeckles. Ref.22 Ref.27

Tissue specificity

Expressed ubiquitously.

Domain

The minimal CTE binding domain consists of an RNP-type RNA binding domain (RBD) and leucine-rich repeats. Ref.29

The nucleoporin binding domain consists of a NTF2 domain (also called NTF2-like domain) and a TAP-C domain (also called UBA-like domain). It has 2 nucleoporin-FG-repeats binding sites (one in the NTF2 and the other in the TAP-C domain) which contribute to nucleoporin association and act synergistically to export cellular mRNAs. Ref.29

The NTF2 domain is functional only in the presence of NXT1 and is essential for the export of mRNA from the nucleus. It inhibits RNA binding activity through an intramolecular interaction with the N-terminal RNA binding domain (RBD); the inhibition is removed by an association with the TREX complex, specifically involving ALYREF/THOC4 and THOC5. Ref.29

The TAP-C domain mediates direct interactions with nucleoporin-FG-repeats and is necessary and sufficient for localization of NXF1 to the nuclear rim. The conserved loop 594-NWD-596 of the TAP-C domain has a critical role in the interaction with nucleoporins. Ref.29

The leucine-rich repeats are essential for the export of mRNA from the nucleus. Ref.29

The RNA-binding domain is a non-canonical RNP-type domain. Ref.29

Sequence similarities

Belongs to the NXF family.

Contains 4 LRR (leucine-rich) repeats.

Contains 1 NTF2 domain.

Contains 1 RRM (RNA recognition motif) domain.

Contains 1 TAP-C domain.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9UBU9-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q9UBU9-2)

The sequence of this isoform differs from the canonical sequence as follows:
     339-356: SAIRERFPKLLRLDGHEL → RSVVACVSPPGDLHPLGG
     357-619: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.19
Chain2 – 619618Nuclear RNA export factor 1
PRO_0000220529

Regions

Domain119 – 19880RRM
Repeat266 – 29126LRR 1
Repeat292 – 31524LRR 2
Repeat316 – 34328LRR 3
Repeat344 – 37128LRR 4
Domain386 – 536151NTF2
Domain565 – 61955TAP-C
Region2 – 198197Interaction with ALYREF/THOC4
Region2 – 118117RNA-binding (RBD)
Region2 – 6059Minor non-specific RNA-binding
Region61 – 11858Major non-specific RNA-binding
Motif67 – 10034Nuclear localization signal
Motif83 – 11028Nuclear export signal
Compositional bias551 – 56111Pro-rich

Amino acid modifications

Modified residue21N-acetylalanine Ref.19
Modified residue1261Nitrated tyrosine By similarity

Natural variations

Alternative sequence339 – 35618SAIRE…DGHEL → RSVVACVSPPGDLHPLGG in isoform 2.
VSP_041427
Alternative sequence357 – 619263Missing in isoform 2.
VSP_041428

Experimental info

Mutagenesis711R → A: Greatly reduces RNA binding and no effect on interaction with ALYREF/THOC4; when associated with A-78, A-81, A-82, A-89, A-91, A-97, A-98, A-100 and A-105. Ref.18
Mutagenesis781R → A: Greatly reduces RNA binding and no effect on interaction with ALYREF/THOC4; when associated with A-71, A-81, A-82, A-89, A-91, A-97, A-98, A-100 and A-105. Ref.18
Mutagenesis811R → A: Greatly reduces RNA binding and no effect on interaction with ALYREF/THOC4; when associated with A-71, A-78, A-82, A-89, A-91, A-97, A-98, A-100 and A-105. Ref.18
Mutagenesis821R → A: Greatly reduces RNA binding and no effect on interaction with ALYREF/THOC4; when associated with A-71, A-78, A-81, A-89, A-91, A-97, A-98, A-100 and A-105. Ref.18
Mutagenesis891R → A: Greatly reduces RNA binding and no effect on interaction with ALYREF/THOC4; when associated with A-71, A-78, A-81, A-82, A-91, A-97, A-98, A-100 and A-105. Ref.18
Mutagenesis911R → A: Greatly reduces RNA binding and no effect on interaction with ALYREF/THOC4; when associated with A-71, A-78, A-81, A-82, A-89, A-97, A-98, A-100 and A-105. Ref.18
Mutagenesis971R → A: Greatly reduces RNA binding and no effect on interaction with ALYREF/THOC4; when associated with A-71, A-78, A-81, A-82, A-89, A-91, A-98, A-100 and A-105. Ref.18
Mutagenesis981R → A: Greatly reduces RNA binding and no effect on interaction with ALYREF/THOC4; when associated with A-71, A-78, A-81, A-82, A-89, A-91, A-97, A-100 and A-105. Ref.18
Mutagenesis1001R → A: Greatly reduces RNA binding and no effect on interaction with ALYREF/THOC4; when associated with A-71, A-78, A-81, A-82, A-89, A-91, A-97, A-98 and A-105. Ref.18
Mutagenesis1051R → A: Greatly reduces RNA binding and no effect on interaction with ALYREF/THOC4; when associated with A-71, A-78, A-81, A-82, A-89, A-91, A-97, A-98 and A-100. Ref.18
Mutagenesis306 – 3083ERE → AAA: Decreases the export of mRNAs from the nucleus.
Mutagenesis3831L → R: Diminishes nuclear rim staining and 80% reduction in mRNA export activity; when associated with R-386. Complete loss of nuclear rim staining and mRNA export activity; when associated with R-386 and A-594. Ref.29
Mutagenesis3861L → R: Diminishes nuclear rim staining and 80% reduction in mRNA export activity; when associated with R-383. Complete loss of nuclear rim staining and mRNA export activity; when associated with R-383 and A-594. Ref.29
Mutagenesis3991D → A: 60% reduction in mRNA export activity. Ref.29
Mutagenesis450 – 4534LRFR → AAAA: Abolishes interaction with THOC5 and CHTOP. Ref.25 Ref.26
Mutagenesis4531R → A: Impairs intramolecular interaction between RBD and NTF2. Ref.25
Mutagenesis456 – 4594KHTR → AAAA: Abolishes interaction with THOC5 and CHTOP, no effect on interaction with NXT1; enhances intramolecular interaction between RBD and NTF2, reduces RNA binding and mRNA export. Ref.25 Ref.26
Mutagenesis4561K → D: Impairs intramolecular interaction between RBD and NTF2; when associated with D-459.
Mutagenesis4591R → D: Impairs intramolecular interaction between RBD and NTF2; when associated with D-456.
Mutagenesis4821D → R: 90% reduction in mRNA export activity. Ref.29
Mutagenesis5181I → R: 98% reduction in mRNA export activity. Ref.29
Mutagenesis5211P → Q: 35% reduction in mRNA export activity. Ref.29
Mutagenesis5941W → A: Suppresses FG-nucleoporin binding. Diminishes nuclear rim staining and 88% reduction in mRNA export activity. Complete loss of nuclear rim staining and mRNA export activity; when associated with R-383 and R-386. Ref.29
Mutagenesis5951D → R: Suppresses FG-nucleoporin binding.
Mutagenesis6171F → A: Suppresses FG-nucleoporin binding. Ref.31
Sequence conflict1191W → C in AAB81111. Ref.8
Sequence conflict2561T → N in AAD20016. Ref.3

Secondary structure

.......................................................................................... 619
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 338872AADA789FBF

FASTA61970,182
        10         20         30         40         50         60 
MADEGKSYSE HDDERVNFPQ RKKKGRGPFR WKYGEGNRRS GRGGSGIRSS RLEEDDGDVA 

        70         80         90        100        110        120 
MSDAQDGPRV RYNPYTTRPN RRGDTWHDRD RIHVTVRRDR APPERGGAGT SQDGTSKNWF 

       130        140        150        160        170        180 
KITIPYGRKY DKAWLLSMIQ SKCSVPFTPI EFHYENTRAQ FFVEDASTAS ALKAVNYKIL 

       190        200        210        220        230        240 
DRENRRISII INSSAPPHTI LNELKPEQVE QLKLIMSKRY DGSQQALDLK GLRSDPDLVA 

       250        260        270        280        290        300 
QNIDVVLNRR SCMAATLRII EENIPELLSL NLSNNRLYRL DDMSSIVQKA PNLKILNLSG 

       310        320        330        340        350        360 
NELKSERELD KIKGLKLEEL WLDGNSLCDT FRDQSTYISA IRERFPKLLR LDGHELPPPI 

       370        380        390        400        410        420 
AFDVEAPTTL PPCKGSYFGT ENLKSLVLHF LQQYYAIYDS GDRQGLLDAY HDGACCSLSI 

       430        440        450        460        470        480 
PFIPQNPARS SLAEYFKDSR NVKKLKDPTL RFRLLKHTRL NVVAFLNELP KTQHDVNSFV 

       490        500        510        520        530        540 
VDISAQTSTL LCFSVNGVFK EVDGKSRDSL RAFTRTFIAV PASNSGLCIV NDELFVRNAS 

       550        560        570        580        590        600 
SEEIQRAFAM PAPTPSSSPV PTLSPEQQEM LQAFSTQSGM NLEWSQKCLQ DNNWDYTRSA 

       610 
QAFTHLKAKG EIPEVAFMK 

« Hide

Isoform 2 [UniParc].

Checksum: 470701F5324EC0B5
Show »

FASTA35640,476

References

« Hide 'large scale' references
[1]"TAP binds to the constitutive transport element (CTE) through a novel RNA-binding motif that is sufficient to promote CTE-dependent RNA export from the nucleus."
Braun I.C., Rohrbach E., Schmitt C., Izaurralde E.
EMBO J. 18:1953-1965(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), MUTAGENESIS.
Tissue: Cervix carcinoma.
[2]"The human Tap protein is a nuclear mRNA export factor that contains novel RNA-binding and nucleocytoplasmic transport sequences."
Kang Y., Cullen B.R.
Genes Dev. 13:1126-1139(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]"Identification of novel import and export signals of human TAP, the protein that binds to the constitutive transport element of the type D retrovirus mRNAs."
Bear J., Tan W., Zolotukhin A.S., Tabernero C., Hudson E.A., Felber B.K.
Mol. Cell. Biol. 19:6306-6317(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[4]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
Tissue: Lung and Trachea.
[5]"Human chromosome 11 DNA sequence and analysis including novel gene identification."
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G. expand/collapse author list , Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., Sakaki Y.
Nature 440:497-500(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Brain and Placenta.
[8]"Tap: a novel cellular protein that interacts with tip of herpesvirus saimiri and induces lymphocyte aggregation."
Yoon D.-W., Lee H., Seol W., DeMaria M., Rosenzweig M., Jung J.U.
Immunity 6:571-582(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 61-619, INTERACTION WITH SAIMIRIINE HERPESVIRUS 2 TIP.
Tissue: Lymphocyte.
[9]"TAP, the human homolog of Mex67p, mediates CTE-dependent RNA export from the nucleus."
Grueter P., Tabernero C., von Kobbe C., Schmitt C., Saavedra C., Bachi A., Wilm M., Felber B.K., Izaurralde E.
Mol. Cell 1:649-659(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[10]"The Mex67p-mediated nuclear mRNA export pathway is conserved from yeast to human."
Katahira J., Straesser K., Podtelejnikov A., Mann M., Jung J.U., Hurt E.
EMBO J. 18:2593-2609(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NUPL2.
[11]"Overexpression of TAP/p15 heterodimers bypasses nuclear retention and stimulates nuclear mRNA export."
Braun I.C., Herold A., Rode M., Conti E., Izaurralde E.
J. Biol. Chem. 276:20536-20543(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
[12]"The C-terminal domain of TAP interacts with the nuclear pore complex and promotes export of specific CTE-bearing RNA substrates."
Bachi A., Braun I.C., Rodrigues J.P., Pante N., Ribbeck K., von Kobbe C., Kutay U., Wilm M., Goerlich D., Carmo-Fonseca M., Izaurralde E.
RNA 6:136-158(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
[13]"Prediction of structural domains of TAP reveals details of its interaction with p15 and nucleoporins."
Suyama M., Doerks T., Braun I.C., Sattler M., Izaurralde E., Bork P.
EMBO Rep. 1:53-58(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS.
[14]"Magoh, a human homolog of Drosophila mago nashi protein, is a component of the splicing-dependent exon-exon junction complex."
Kataoka N., Diem M.D., Kim V.N., Yong J., Dreyfuss G.
EMBO J. 20:6424-6433(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ALYREF/THOC4 AND THE EXON JUNCTION COMPLEX.
[15]"Role of the nonsense-mediated decay factor hUpf3 in the splicing-dependent exon-exon junction complex."
Kim V.N., Kataoka N., Dreyfuss G.
Science 293:1832-1836(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A MRNP COMPLEX WITH UPF3A AND UPF3B.
[16]"Communication of the position of exon-exon junctions to the mRNA surveillance machinery by the protein RNPS1."
Lykke-Andersen J., Shu M.-D., Steitz J.A.
Science 293:1836-1839(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A POST-SPLICING COMPLEX WITH RBM8A; UPF1; UPF2; UPF3A; UPF3B AND RNPS1.
[17]"eIF4A3 is a novel component of the exon junction complex."
Chan C.C., Dostie J., Diem M.D., Feng W., Mann M., Rappsilber J., Dreyfuss G.
RNA 10:200-209(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH EIF4A3 AND ALYREF/THOC4.
[18]"Mutually exclusive interactions drive handover of mRNA from export adaptors to TAP."
Hautbergue G.M., Hung M.L., Golovanov A.P., Lian L.Y., Wilson S.A.
Proc. Natl. Acad. Sci. U.S.A. 105:5154-5159(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF ARG-71; ARG-78; ARG-81; ARG-82; ARG-89; ARG-91; ARG-97; ARG-98; ARG-100 AND ARG-105.
[19]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[20]"UIF, a new mRNA export adaptor that works together with REF/ALY, requires FACT for recruitment to mRNA."
Hautbergue G.M., Hung M.L., Walsh M.J., Snijders A.P., Chang C.T., Jones R., Ponting C.P., Dickman M.J., Wilson S.A.
Curr. Biol. 19:1918-1924(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH FYTTD1.
[21]"Adaptor Aly and co-adaptor Thoc5 function in the Tap-p15-mediated nuclear export of HSP70 mRNA."
Katahira J., Inoue H., Hurt E., Yoneda Y.
EMBO J. 28:556-567(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH ALYREF/THOC4 AND THOC5.
[22]"Assembly and mobility of exon-exon junction complexes in living cells."
Schmidt U., Im K.-B., Benzing C., Janjetovic S., Rippe K., Lichter P., Wachsmuth M.
RNA 15:862-876(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[23]"The cellular RNA export receptor TAP/NXF1 is required for ICP27-mediated export of herpes simplex virus 1 RNA, but the TREX complex adaptor protein Aly/REF appears to be dispensable."
Johnson L.A., Li L., Sandri-Goldin R.M.
J. Virol. 83:6335-6346(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HUMAN HERPES VIRUS 1 ICP27.
[24]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[25]"TREX exposes the RNA-binding domain of Nxf1 to enable mRNA export."
Viphakone N., Hautbergue G.M., Walsh M., Chang C.T., Holland A., Folco E.G., Reed R., Wilson S.A.
Nat. Commun. 3:1006-1006(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ASSOCIATION WITH THE TREX COMPLEX, RNA-BINDING, MUTAGENESIS OF ARG-453 AND 456-LYS--ARG-459.
[26]"Chtop is a component of the dynamic TREX mRNA export complex."
Chang C.T., Hautbergue G.M., Walsh M.J., Viphakone N., van Dijk T.B., Philipsen S., Wilson S.A.
EMBO J. 32:473-486(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CHTOP; THOC5 AND ALYREF, MUTAGENESIS OF 450-LEU--ARG-453 AND 456-LYS--ARG-459.
[27]"Mapping interactions between mRNA export factors in living cells."
Teng I.F., Wilson S.A.
PLoS ONE 8:E67676-E67676(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH CHTOP.
[28]"The structure of the mRNA export factor TAP reveals a cis arrangement of a non-canonical RNP domain and an LRR domain."
Liker E., Fernandez E., Izaurralde E., Conti E.
EMBO J. 19:5587-5598(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 102-372.
[29]"Structural basis for the recognition of a nucleoporin FG repeat by the NTF2-like domain of the TAP/p15 mRNA nuclear export factor."
Fribourg S., Braun I.C., Izaurralde E., Conti E.
Mol. Cell 8:645-656(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH NXT1, X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH NXT1-FG-REPEAT, SUBUNIT, DOMAINS, MUTAGENESIS OF LEU-383; LEU-386; ASP-399; ASP-482; ILE-518; PRO-521 AND TRP-594.
[30]"Structural basis for the interaction between the Tap/NXF1 UBA domain and FG nucleoporins at 1A resolution."
Grant R.P., Neuhaus D., Stewart M.
J. Mol. Biol. 326:849-858(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.0 ANGSTROMS) OF 561-619 IN COMPLEX WITH RANBP3.
[31]"Structure of the C-terminal FG-nucleoporin binding domain of Tap/NXF1."
Grant R.P., Hurt E., Neuhaus D., Stewart M.
Nat. Struct. Biol. 9:247-251(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 551-619, MUTAGENESIS OF PHE-617.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ132712 mRNA. Translation: CAA10753.1.
AF112880 mRNA. Translation: AAD39102.1.
AF126246 mRNA. Translation: AAD20016.1.
AK304137 mRNA. Translation: BAG65031.1.
AK027192 mRNA. No translation available.
AP001160 Genomic DNA. No translation available.
CH471076 Genomic DNA. Translation: EAW74105.1.
BC004904 mRNA. Translation: AAH04904.1.
BC028041 mRNA. Translation: AAH28041.1.
U80073 mRNA. Translation: AAB81111.1.
RefSeqNP_001074960.1. NM_001081491.1.
NP_006353.2. NM_006362.4.
UniGeneHs.523739.
Hs.601546.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1FO1X-ray2.90A/B102-372[»]
1FT8X-ray3.15A/B/C/D/E102-372[»]
1GO5NMR-A551-619[»]
1JKGX-ray1.90B371-619[»]
1JN5X-ray2.80B371-619[»]
1KOHX-ray3.80A/B/C/D96-372[»]
1KOOX-ray3.80A/B/C/D96-372[»]
1OAIX-ray1.00A561-619[»]
2Z5KX-ray2.60B53-82[»]
2Z5MX-ray3.00B53-82[»]
3RW6X-ray2.30A/B96-362[»]
3RW7X-ray3.00A/B/C/D96-362[»]
ProteinModelPortalQ9UBU9.
SMRQ9UBU9. Positions 118-362, 371-619.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115745. 91 interactions.
DIPDIP-31789N.
IntActQ9UBU9. 52 interactions.
MINTMINT-121360.
STRING9606.ENSP00000294172.

Protein family/group databases

TCDB3.A.18.1.1. the nuclear mrna exporter (mrna-e) family.

PTM databases

PhosphoSiteQ9UBU9.

Polymorphism databases

DMDM20139282.

Proteomic databases

PaxDbQ9UBU9.
PeptideAtlasQ9UBU9.
PRIDEQ9UBU9.

Protocols and materials databases

DNASU10482.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000294172; ENSP00000294172; ENSG00000162231. [Q9UBU9-1]
ENST00000439713; ENSP00000408864; ENSG00000162231. [Q9UBU9-2]
ENST00000531709; ENSP00000453885; ENSG00000162231. [Q9UBU9-2]
ENST00000532297; ENSP00000436679; ENSG00000162231. [Q9UBU9-1]
GeneID10482.
KEGGhsa:10482.
UCSCuc001nvf.1. human. [Q9UBU9-1]
uc001nvg.1. human. [Q9UBU9-2]

Organism-specific databases

CTD10482.
GeneCardsGC11M062559.
HGNCHGNC:8071. NXF1.
HPACAB016327.
MIM602647. gene.
neXtProtNX_Q9UBU9.
PharmGKBPA31858.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG324438.
HOGENOMHOG000236269.
HOVERGENHBG013199.
InParanoidQ9UBU9.
KOK14284.
OMADQENRRI.
OrthoDBEOG7QZGB9.
PhylomeDBQ9UBU9.
TreeFamTF314566.

Enzyme and pathway databases

ReactomeREACT_71. Gene Expression.

Gene expression databases

ArrayExpressQ9UBU9.
BgeeQ9UBU9.
CleanExHS_NXF1.
GenevestigatorQ9UBU9.

Family and domain databases

Gene3D3.30.70.330. 1 hit.
InterProIPR001611. Leu-rich_rpt.
IPR002075. NTF2.
IPR018222. Nuclear_transport_factor_2_euk.
IPR012677. Nucleotide-bd_a/b_plait.
IPR005637. TAP_C_dom.
IPR015245. Tap_RNA-bd.
IPR003603. U2A'_phosphoprotein32A_C.
IPR009060. UBA-like.
[Graphical view]
PfamPF00560. LRR_1. 1 hit.
PF02136. NTF2. 1 hit.
PF09162. Tap-RNA_bind. 1 hit.
PF03943. TAP_C. 1 hit.
[Graphical view]
ProDomPD043466. Tap_RNA_bd. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00446. LRRcap. 1 hit.
SM00804. TAP_C. 1 hit.
[Graphical view]
SUPFAMSSF46934. SSF46934. 1 hit.
PROSITEPS51450. LRR. 3 hits.
PS50177. NTF2_DOMAIN. 1 hit.
PS51281. TAP_C. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSNXF1. human.
EvolutionaryTraceQ9UBU9.
GeneWikiNXF1.
GenomeRNAi10482.
NextBio39766.
PROQ9UBU9.
SOURCESearch...

Entry information

Entry nameNXF1_HUMAN
AccessionPrimary (citable) accession number: Q9UBU9
Secondary accession number(s): B4E269, Q99799, Q9UQL2
Entry history
Integrated into UniProtKB/Swiss-Prot: March 27, 2002
Last sequence update: May 1, 2000
Last modified: April 16, 2014
This is version 159 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM